Construction and preliminary characterization of three hemagglutinin mutants of Porphyromonas gingivalis

Lépine, Guylaine; Ellen, Richard P.; Progulske‐Fox, Ann

doi:10.1128/iai.64.4.1467-1472.1996

Cited by 43 publications

(38 citation statements)

References 27 publications

(31 reference statements)

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“…Hemagglutinins/adhesions not only mediate the adsorption and invasion of bacteria into host cells, but also take part in iron/heme utilization [96][97][98]. P. gingivalis possesses five major hemagglutinin genes (hagA, hagB, hagC, hagD and hagE) [99]. The gene sequences for six newly identified putative hemagglutinin-like proteins have also been identified in the P. gingivalis W83 genome (Table 1) [20].…”

Section: Hemagglutinins and Hemolysinsmentioning

confidence: 99%

Iron and heme utilization inPorphyromonas gingivalis

et al. 2005

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Porphyromonas gingivalis is a Gram-negative anaerobic bacterium associated with the initiation and progression of adult periodontal disease. Iron is utilized by this pathogen in the form of heme and has been shown to play an essential role in its growth and virulence. Recently, considerable attention has been given to the characterization of various secreted and surface-associated proteins of P. gingivalis and their contribution to virulence. In particular, the properties of proteins involved in the uptake of iron and heme have been extensively studied. Unlike other Gram-negative bacteria, P. gingivalis does not produce siderophores. Instead it employs specific outer membrane receptors, proteases (particularly gingipains), and lipoproteins to acquire iron/heme. In this review, we will focus on the diverse mechanisms of iron and heme acquisition in P. gingivalis. Specific proteins involved in iron and heme capture will be described. In addition, we will discuss new genes for iron/heme utilization identified by nucleotide sequencing of the P. gingivalis W83 genome. Putative iron- and heme-responsive gene regulation in P. gingivalis will be discussed. We will also examine the significance of heme/hemoglobin acquisition for the virulence of this pathogen.

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Section: Hemagglutinins and Hemolysinsmentioning

confidence: 99%

Iron and heme utilization inPorphyromonas gingivalis

et al. 2005

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“…Spe-ci®c antibodies to HA-Ag2 have been shown to inhibit haemagglutination and binding of P. gingivalis to epithelial cells (28,49,315). A number of studies have identi®ed four P. gingivalis genes that encode haemagglutinin proteins HagA, B, C, and D (191,192,278,279). Research into these four Hag proteins has focused on HagA and B with particular interest in HagB as a potential vaccine candidate.…”

Section: Haemagglutininsmentioning

confidence: 99%

Antigens of bacteria associated with periodontitis

O'Brien-Simpson¹,

Veith²,

Dashper³

et al. 2004

Periodontology 2000

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“…Nelson et al (2003),Dashper et al (2000),Hendtlass et al . (1996),Lepine et al (1996),Slakeski et al (1999),Nelson et al (2003),Smalley et al (2006),Nhien et al . (1995),Aduse-Opoku et al (1995),Slakeski et al (1996), Rangarajan et al (1997), Nelson et al (2003), Nhien et al (2010), Watanabe et al (2011), Siddiqui et al (2014), Yang et al (2015), Smalley et al .…”

mentioning

confidence: 99%

Heme acquisition mechanisms of Porphyromonas gingivalis – strategies used in a polymicrobial community in a heme‐limited host environment

Smalley

Olczak

2016

Molecular Oral Microbiology

137

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Summary Porphyromonas gingivalis, a main etiologic agent and key pathogen responsible for initiation and progression of chronic periodontitis requires heme as a source of iron and protoporphyrin IX for its survival and the ability to establish an infection. Porphyromonas gingivalis is able to accumulate a defensive cell‐surface heme‐containing pigment in the form of μ‐oxo bisheme. The main sources of heme for P. gingivalis in vivo are hemoproteins present in saliva, gingival crevicular fluid, and erythrocytes. To acquire heme, P. gingivalis uses several mechanisms. Among them, the best characterized are those employing hemagglutinins, hemolysins, and gingipains (Kgp, RgpA, RgpB), TonB‐dependent outer‐membrane receptors (HmuR, HusB, IhtA), and hemophore‐like proteins (HmuY, HusA). Proteins involved in intracellular heme transport, storage, and processing are less well characterized (e.g. PgDps). Importantly, P. gingivalis may also use the heme acquisition systems of other bacteria to fulfill its own heme requirements. Porphyromonas gingivalis displays a novel paradigm for heme acquisition from hemoglobin, whereby the Fe(II)‐containing oxyhemoglobin molecule must first be oxidized to methemoglobin to facilitate heme release. This process not only involves P. gingivalis arginine‐ and lysine‐specific gingipains, but other proteases (e.g. interpain A from Prevotella intermedia) or pyocyanin produced by Pseudomonas aeruginosa. Porphyromonas gingivalis is then able to fully proteolyze the more susceptible methemoglobin substrate to release free heme or to wrest heme from it directly through the use of the HmuY hemophore.

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Construction and preliminary characterization of three hemagglutinin mutants of Porphyromonas gingivalis

Cited by 43 publications

References 27 publications

Iron and heme utilization inPorphyromonas gingivalis

Iron and heme utilization inPorphyromonas gingivalis

Antigens of bacteria associated with periodontitis

Heme acquisition mechanisms of Porphyromonas gingivalis – strategies used in a polymicrobial community in a heme‐limited host environment

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